Synthesis of the apoprotein of cytochrome b in heme-deficient yeast cells.

The presence of the apoprotein of cytochrome b has been demonstrated in a mutant of Sacchromyces cerevisiae lacking delta-aminolevulinic acid synthase and, hence, devoid of heme. The apoprotein of cytochrome b present in the mutant was identical with cytochrome b of control cells (mutant cells grown in the presence of delta-aminolevulinic acid) by the following criteria: similar apparent molecular weights in dodecyl sulfate-polyacrylamide gel electrophoresis; anomalous migration behavior during electrophoresis in polyacrylamide gels of different porosities; identical gel pattern obtained after immunoprecipitation with specific antiserum against cytochrome b; and identical fingerprints obtained after limited proteolysis with Staphylococcus aureus V8 protease. The kinetics of incorporation in vivo of [35S]methionine into apoprotein of cytochrome b in the mutant suggested that heme deficiency may affect assembly into the membrane of subunits of the cytochrome b.c1 complex rather than synthesis of cytochrome b.